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Protein adsorption properties of OEG monolayers and dense PNIPAM brushes probed by neutron reflectivity |
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| Authors: | N Brouette C Xue M Haertlein M Moulin G Fragneto DE Leckband A Halperin M Sferrazza |
| Institution: | 1. Département de Physique, Faculté des Sciences, Université Libre de Bruxelles, Boulevard du Triomphe, CP. 223, 1050, Bruxelles, Belgique 2. Department of Chemical and Biomolecular Engineering, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA 3. Institut Max Von Laue-Paul Langevin, 38042, Grenoble, France 4. Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801, USA 5. University of Grenoble 1/CNRS, LIPhy UMR 5588, BP. 87, 38041, Grenoble, France |
| Abstract: | The structure of dense poly(N-isopropylacrylamide) (PNIPAM) brushes and oligo(ethylene glycol) (OEG) monolayers has been probed using neutron reflectometry and ellipsometry. The PNIPAM brush is swollen below the Lower Critical Solution Temperature (LCST) of 32?°C and is collapsed at 37?°C. Neutron reflectivity shows that below the LCST, the brush is described by a two-layer model: an inner dense layer and a hydrated outer layer. Above the LCST the collapsed brush forms a homogenous layer. With a fully deuterated myoglobin protein to increase the neutron scattering length density contrast, the reflectivity data show no detectable primary adsorption on the grafted OEG surface. A bound on the ternary adsorption onto PNIPAM chains forming dense brushes below and above the LCST is obtained. |
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